Biophysical Reviews

, Volume 10, Issue 2, pp 631–640 | Cite as

The versatile mutational “repertoire” of Escherichia coli GroEL, a multidomain chaperonin nanomachine

  • Tomohiro Mizobata
  • Yasushi Kawata


The bacterial chaperonins are highly sophisticated molecular nanomachines, controlled by the hydrolysis of ATP to dynamically trap and remove from the environment unstable protein molecules that are susceptible to denaturation and aggregation. Chaperonins also act to assist in the refolding of these unstable proteins, providing a means by which these proteins may return in active form to the complex environment of the cell. The Escherichia coli GroE chaperonin system is one of the largest protein supramolecular complexes known, whose quaternary structure is required for segregating aggregation-prone proteins. Over the course of more than two decades of research on GroE, it has become accepted that GroE, more specifically the GroEL subunit, is a “high-tolerance” molecular system, capable of accommodating numerous mutations, while retaining its molecular integrity. In some cases, a given site of mutation was revealed to be absolutely required for GroEL function, providing hints regarding the network of signals and triggers that propel this unique system. In other instances, however, a mutation has produced a more delicate response, altering only part of, or in some cases, only a single facet of, the molecular mechanism, and these mutants have often provided invaluable hints on the extent of the complexity underlying chaperonin-assisted protein folding. In this review, we highlight some examples of the latter type of GroEL mutants which compose the unique “mutational repertoire” of GroEL and touch upon the important clues that each mutant provided to the overall effort to elucidate the details of GroE action.


Chaperonin GroEL Molecular nanomachine Versatile mutation 



Portions of the manuscript performed by the authors was funded by a Grant-in-Aid for Scientific Research (C) (no. 22570119 to T. M.) from the Japan Society for the Promotion of Science (JSPS) and by the Strategic Research Program for Brain Sciences from the Japan Agency for Medical Research and Development (AMED).

Compliance with ethical standards

Conflict of interest

Tomohiro Mizobata declares that he has no conflict of interest. Yasushi Kawata declares that he has no conflict of interest.

Ethical approval

This article does not contain any studies with human participants or animals performed by any of the authors.


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Copyright information

© International Union for Pure and Applied Biophysics (IUPAB) and Springer-Verlag GmbH Germany, part of Springer Nature 2017

Authors and Affiliations

  1. 1.Graduate School of Engineering and Graduate School of Medical SciencesTottori UniversityTottoriJapan

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